COBH_SINSX
ID COBH_SINSX Reviewed; 210 AA.
AC P21638;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Precorrin-8X methylmutase;
DE EC=5.4.99.61;
DE AltName: Full=HBA synthase;
DE AltName: Full=Precorrin isomerase;
GN Name=cobH;
OS Sinorhizobium sp.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=42445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SC510;
RX PubMed=2211521; DOI=10.1128/jb.172.10.5980-5990.1990;
RA Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F.,
RA Thibaut D., Debussche L.;
RT "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans
RT fragment carrying eight genes involved in transformation of precorrin-2 to
RT cobyrinic acid.";
RL J. Bacteriol. 172:5980-5990(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-18, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1732194; DOI=10.1128/jb.174.3.1043-1049.1992;
RA Thibaut D., Couder M., Famechon A., Debussche L., Cameron B., Crouzet J.,
RA Blanche F.;
RT "The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed
RT by the cobH gene product with precorrin-8x as the substrate.";
RL J. Bacteriol. 174:1043-1049(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-210 OF APOENZYME AND IN COMPLEX
RP WITH HYDROGENOBYRINATE, SUBUNIT, ACTIVE SITE, AND REACTION MECHANISM.
RX PubMed=11470433; DOI=10.1016/s0969-2126(01)00618-9;
RA Shipman L.W., Li D., Roessner C.A., Scott A.I., Sacchettini J.C.;
RT "Crystal structure of precorrin-8x methyl mutase.";
RL Structure 9:587-596(2001).
CC -!- FUNCTION: Catalyzes the conversion of precorrin-8X to
CC hydrogenobyrinate. {ECO:0000269|PubMed:1732194}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + precorrin-8X = hydrogenobyrinate;
CC Xref=Rhea:RHEA:22512, ChEBI:CHEBI:15378, ChEBI:CHEBI:58581,
CC ChEBI:CHEBI:77873; EC=5.4.99.61;
CC Evidence={ECO:0000269|PubMed:1732194};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.91 uM for precorrin-8X {ECO:0000269|PubMed:1732194};
CC Vmax=230 nmol/h/mg enzyme {ECO:0000269|PubMed:1732194};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 8/10.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11470433}.
CC -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from Pseudomonas
CC denitrificans, but similarity searches show that the sequence is much
CC closer to Sinorhizobium. The entry's taxonomy has been changed.
CC {ECO:0000305}.
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DR EMBL; M59301; AAA25796.1; -; Genomic_DNA.
DR PDB; 1F2V; X-ray; 2.10 A; A=2-210.
DR PDB; 1I1H; X-ray; 2.60 A; A=2-210.
DR PDBsum; 1F2V; -.
DR PDBsum; 1I1H; -.
DR AlphaFoldDB; P21638; -.
DR SMR; P21638; -.
DR DrugBank; DB02460; Hydrogenobyrinic acid.
DR KEGG; ag:AAA25796; -.
DR BioCyc; MetaCyc:MON-115; -.
DR SABIO-RK; P21638; -.
DR UniPathway; UPA00148; UER00219.
DR EvolutionaryTrace; P21638; -.
DR GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10230; -; 1.
DR InterPro; IPR003722; Cbl_synth_CobH/CbiC.
DR InterPro; IPR036588; CobH/CbiC_sf.
DR Pfam; PF02570; CbiC; 1.
DR SUPFAM; SSF63965; SSF63965; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Direct protein sequencing; Isomerase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1732194"
FT CHAIN 2..210
FT /note="Precorrin-8X methylmutase"
FT /id="PRO_0000135926"
FT ACT_SITE 43
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:11470433"
FT BINDING 17
FT /ligand="substrate"
FT BINDING 40
FT /ligand="substrate"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1I1H"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:1F2V"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1F2V"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:1F2V"
SQ SEQUENCE 210 AA; 22064 MW; 506D1C4C5D972B3F CRC64;
MPEYDYIRDG NAIYERSFAI IRAEADLSRF SEEEADLAVR MVHACGSVEA TRQFVFSPDF
VSSARAALKA GAPILCDAEM VAHGVTRARL PAGNEVICTL RDPRTPALAA EIGNTRSAAA
LKLWSERLAG SVVAIGNAPT ALFFLLEMLR DGAPKPAAIL GMPVGFVGAA ESKDALAENS
YGVPFAIVRG RLGGSAMTAA ALNSLARPGL
